期刊
TOXICON
卷 53, 期 6, 页码 685-692出版社
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.toxicon.2009.02.001
关键词
Phospholipase A(2); PLA(2); Phospholipase A(2) inhibitor; PLI; Colubridae; cDNA sequence
资金
- Ministry of Education, Science, Sports, and Culture of Japan [12672137]
- Grants-in-Aid for Scientific Research [12672137] Funding Source: KAKEN
Two distinct phospholipase A(2) (PLA(2)) inhibitory proteins (PLIs) were purified from the serum of the Japanese rat snake, Elaphe climacophora. The 150-kDa inhibitor, a trimer of a 50-kDa subunit, specifically inhibited the basic PLA(2) purified from the venom of Gloydius brevicaudus, whereas the 120-kDa one composed of two distinct 25-kDa subunits, A and B, inhibited both the acidic and basic PLA(2)S of G. brevicaudus. On the basis of their amino acid sequences, these inhibitors were assigned as PLI beta and PLI gamma, respectively. A PLI alpha homolog (PLI alpha-like protein; PLI alpha-LP) having an apparent molecular weight of 50-kDa and composed of 15-kDa subunits was also purified from the E climacophora serum. This homolog was immunoreactive with antibody raised against the G. brevicaudus PLI alpha, but lacked in the inhibitory activity toward the acidic and basic PLA(2)s. The cDNAs encoding PLI alpha-LP, PLI beta, PLI gamma-A, and PLI gamma-B were cloned from liver RNA, and their nucleotide sequences were compared with those of other venomous and non-venomous snakes. (C) 2009 Elsevier Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据